Evidence map›Paper›PMID 40645829›Full record

ReviewTrends in biochemical sciences2025

The ribosome ubiquitination code: fine-tuning translation under stress.

Haleigh C Wooters, Neil C Nimmagadda, Alicia M Darnell, Gustavo M Silva

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Haleigh C WootersDepartment of Biology, Duke University, Durham, NC 27708, USA.
Neil C NimmagaddaDepartment of Biology, Duke University, Durham, NC 27708, USA.
Alicia M DarnellDepartment of Pharmacology and Cancer Biology, School of Medicine, Duke University, Durham, NC 27708, USA.
Gustavo M SilvaDepartment of Biology, Duke University, Durham, NC 27708, USA. Electronic address: gustavo.silva@duke.edu.

Funding

Dissecting the roles of ubiquitin in translation controlR35GM137954 · NIGMS · DUKE UNIVERSITY · PI Gustavo M Silva · 2020 to 2026
$3.0M
NIGMS NIH HHS R35 GM137954
6 · The paper itself

Abstract

It has become evident that a complex code of ribosome ubiquitination regulates protein synthesis, particularly in stress conditions. Ubiquitin is known largely for its role in protein stability; however, new high-throughput screening and advances in proteomics are underscoring its novel role as a master regulator of ribosome function. Still, much remains to be discovered about how this code acts and supports translation reprogramming in a context-specific manner. Here we discuss the nature of this code, the dynamics of site-specific ribosome ubiquitination, and the unique roles that multiple enzymes play in defining the translatome and cotranslational quality control pathways. We also provide insights on the importance of unraveling this code to understand the physiological impact of modified ribosome subpopulations in cellular stress and human disease.

Indexed as

Protein BiosynthesisRibosomesStress, PhysiologicalUbiquitinationAnimalsHumanselongation controlquality controlstress responsetranslation reprogrammingubiquitination

Identifiers

PMID40645829
PMCPMC12373267

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.